Albert Jeltsch

Prof. of Biochemistry

University of Stuttgart

Germany

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Professor Albert Jeltsch is a faculty member in the Department of Biochemistry at Universität Stuttgart, Germany. His research focuses on epigenetics, specifically investigating the mechanisms of DNA methylation and demethylation, as well as the activity and specificity of various histone and DNA-modifying enzymes. Recently, he has published articles on topics including the dual specificity of the PRDM9 protein, the development of sensors for cellular histone dynamics, and allele-specific gene expression regulation.

Articles (24)

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2025

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2022

Collaborators (5)

Nicole Radde

University of Stuttgart

GERMANY

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Florian Meyer

University of Stuttgart

GERMANY

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Anja Koehler

University of Stuttgart

GERMANY

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Alex de Mendoza

University of Western Australia

AUSTRALIA

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Monilola A. Olayioye

GERMANY

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Albert Jeltsch

Research Interests

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About

Articles (24)

Development of a BiAD Sensor for Locus-Specific Detection of Cellular Histone Acetylation Dynamics by Fluorescence Microscopy

Investigation and design of the dual specificity of the PRDM9 protein lysine methyltransferase

Dual DNA demethylation mechanisms implement epigenetic memory driven by the pioneer factor PAX7

Systematic analysis of specificities and flanking sequence preferences of bacterial DNA-(cytosine C5)-methyltransferases reveals mechanisms of enzyme- and sequence-specific DNA readout

Allele-specific DNA demethylation editing leads to stable upregulation of allele-specific gene expression

Erratum for the Perspective "Phylogeny of Methylomes" by A. Jeltsch

Discovery of NSD2 non-histone substrates and design of a super-substrate

Specific DNMT3C flanking sequence preferences facilitate methylation of young murine retrotransposons

Modular dual-color BiAD sensors for locus-specific readout of epigenome modifications in single cells

Repeat DNA methylation is modulated by adherens junction signaling

Approaching the catalytic mechanism of protein lysine methyltransferases by biochemical and simulation techniques

Distinct specificities of the HEMK2 protein methyltransferase in methylation of glutamine and lysine residues

Locus-Specific and Stable DNA Demethylation at the H19/IGF2 ICR1 by Epigenome Editing Using a dCas9-SunTag System and the Catalytic Domain of TET1

SETDB1 activity is globally directed by H3K14 acetylation via its Triple Tudor Domain

Refined read‐out: The hUHRF1 Tandem‐Tudor domain prefers binding to histone H3 tails containing K4me1 in the context of H3K9me2/3

On the accuracy of the epigenetic copy machine: comprehensive specificity analysis of the DNMT1 DNA methyltransferase

Limited choice of natural amino acids as mimetics restricts design of protein lysine methylation studies

The R736H cancer mutation in DNMT3A modulates the properties of the FF-subunit interface

Reversible switching and stability of the epigenetic memory system in bacteria

Genome-wide deposition of 6-methyladenine in human DNA reduces the viability of HEK293 cells and directly influences gene expression

Mechanistic basis of the increased methylation activity of the SETD2 protein lysine methyltransferase towards a designed super-substrate peptide

The H3.3 G34W oncohistone mutation increases K36 methylation by the protein lysine methyltransferase NSD1

Special Issue “Structure, Activity, and Function of Protein Methyltransferases”

Methylation of recombinant mononucleosomes by DNMT3A demonstrates efficient linker DNA methylation and a role of H3K36me3

Collaborators (5)

Nicole Radde

Florian Meyer

Anja Koehler

Alex de Mendoza

Monilola A. Olayioye

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